Results 151 to 160 of about 45,557 (210)
Bio-encapsulation of allergen-derivatives for specific immunotherapy. [PDF]
Schubert F +6 more
europepmc +1 more source
Thalamic Activity Regulates Interneuron Density in the Developing Visual Thalamus. [PDF]
Huerga-Gómez I +5 more
europepmc +1 more source
Ferrets as a model for investigating the impact of chemical agents on cerebral cortical sulcogyrogenesis. [PDF]
Sawada K.
europepmc +1 more source
Imipenem in the Rat Brain: A Multidimensional Study on Hippocampal Behavior, GABAergic System, Astrocyte Response, and Neurogenesis. [PDF]
Araújo-Andrade L +8 more
europepmc +1 more source
Methodology for human-induced pluripotent stem cell-derived excitatory and inhibitory neuron coculture with astrocytes for Alzheimer's disease modelling. [PDF]
Li J +7 more
europepmc +1 more source
Some of the next articles are maybe not open access.
Related searches:
Related searches:
Parvalbumin immunoreactivity in the rat retina
Neuroscience Letters, 1990The distribution of the Ca2+ binding protein parvalbumin was studied in the rat retina with immunocytochemistry using a mouse monoclonal antibody. Specific parvalbumin immunoreactivity was identified within a subpopulation of ganglion cells and a subpopulation of amacrine cells.
Pietro Paolo Sanna +2 more
exaly +3 more sources
Journal of Neurochemistry, 1985
Abstract: Parvalbumin was isolated from human cerebral cortex and biceps and triceps muscles by HPLC. The immunological properties of the human protein and the mobility in two‐dimensional polyacrylamide gels were similar to that of parvalbumin isolated from the muscles of rat, mouse, rabbit, and chicken.
M W, Berchtold +2 more
openaire +2 more sources
Abstract: Parvalbumin was isolated from human cerebral cortex and biceps and triceps muscles by HPLC. The immunological properties of the human protein and the mobility in two‐dimensional polyacrylamide gels were similar to that of parvalbumin isolated from the muscles of rat, mouse, rabbit, and chicken.
M W, Berchtold +2 more
openaire +2 more sources
Parvalbumin as a Pleomorphic Protein
Current Protein & Peptide Science, 2017Parvalbumin (PA) is a classical small, mostly cytosolic Ca2+-binding protein of the EF-hand superfamily expressed in vertebrates in a tissue- and cell-specific manner, serving as a magnesium/ calcium buffer. In the last decade novel data were published on structural peculiarities of PA, likely affecting its functionality.
Permyakov, Eugene +2 more
openaire +3 more sources

